Characterization of a Dye-Decolorizing Peroxidase from <i>Irpex lacteus</i> Expressed in <i>Escherichia coli</i>: An Enzyme with Wide Substrate Specificity Able to Transform Lignosulfonates
A dye-decolorizing peroxidase (DyP) from <i>Irpex lacteus</i> was cloned and heterologously expressed as inclusion bodies in <i>Escherichia coli</i>. The protein was purified in one chromatographic step after its in vitro activation. It was active on ABTS, 2,6-dimethoxyphenol...
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MDPI AG
2021-04-01
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author | Laura Isabel de Eugenio Rosa Peces-Pérez Dolores Linde Alicia Prieto Jorge Barriuso Francisco Javier Ruiz-Dueñas María Jesús Martínez |
author_facet | Laura Isabel de Eugenio Rosa Peces-Pérez Dolores Linde Alicia Prieto Jorge Barriuso Francisco Javier Ruiz-Dueñas María Jesús Martínez |
author_sort | Laura Isabel de Eugenio |
collection | DOAJ |
description | A dye-decolorizing peroxidase (DyP) from <i>Irpex lacteus</i> was cloned and heterologously expressed as inclusion bodies in <i>Escherichia coli</i>. The protein was purified in one chromatographic step after its in vitro activation. It was active on ABTS, 2,6-dimethoxyphenol (DMP), and anthraquinoid and azo dyes as reported for other fungal DyPs, but it was also able to oxidize Mn<sup>2+</sup> (as manganese peroxidases and versatile peroxidases) and veratryl alcohol (VA) (as lignin peroxidases and versatile peroxidases). This corroborated that <i>I. lacteus</i> DyPs are the only enzymes able to oxidize high redox potential dyes, VA and Mn<sup>+2</sup>. Phylogenetic analysis grouped this enzyme with other type D-DyPs from basidiomycetes. In addition to its interest for dye decolorization, the results of the transformation of softwood and hardwood lignosulfonates suggest a putative biological role of this enzyme in the degradation of phenolic lignin. |
first_indexed | 2024-03-10T12:03:48Z |
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institution | Directory Open Access Journal |
issn | 2309-608X |
language | English |
last_indexed | 2024-03-10T12:03:48Z |
publishDate | 2021-04-01 |
publisher | MDPI AG |
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series | Journal of Fungi |
spelling | doaj.art-6c703d0444594bec9d5e5aa199896d612023-11-21T16:45:38ZengMDPI AGJournal of Fungi2309-608X2021-04-017532510.3390/jof7050325Characterization of a Dye-Decolorizing Peroxidase from <i>Irpex lacteus</i> Expressed in <i>Escherichia coli</i>: An Enzyme with Wide Substrate Specificity Able to Transform LignosulfonatesLaura Isabel de Eugenio0Rosa Peces-Pérez1Dolores Linde2Alicia Prieto3Jorge Barriuso4Francisco Javier Ruiz-Dueñas5María Jesús Martínez6Centro de Investigaciones Biológicas Margarita Salas (CIB), Consejo Superior de Investigaciones Científicas (CSIC), Ramiro de Maeztu 9, 28040 Madrid, SpainCentro de Investigaciones Biológicas Margarita Salas (CIB), Consejo Superior de Investigaciones Científicas (CSIC), Ramiro de Maeztu 9, 28040 Madrid, SpainCentro de Investigaciones Biológicas Margarita Salas (CIB), Consejo Superior de Investigaciones Científicas (CSIC), Ramiro de Maeztu 9, 28040 Madrid, SpainCentro de Investigaciones Biológicas Margarita Salas (CIB), Consejo Superior de Investigaciones Científicas (CSIC), Ramiro de Maeztu 9, 28040 Madrid, SpainCentro de Investigaciones Biológicas Margarita Salas (CIB), Consejo Superior de Investigaciones Científicas (CSIC), Ramiro de Maeztu 9, 28040 Madrid, SpainCentro de Investigaciones Biológicas Margarita Salas (CIB), Consejo Superior de Investigaciones Científicas (CSIC), Ramiro de Maeztu 9, 28040 Madrid, SpainCentro de Investigaciones Biológicas Margarita Salas (CIB), Consejo Superior de Investigaciones Científicas (CSIC), Ramiro de Maeztu 9, 28040 Madrid, SpainA dye-decolorizing peroxidase (DyP) from <i>Irpex lacteus</i> was cloned and heterologously expressed as inclusion bodies in <i>Escherichia coli</i>. The protein was purified in one chromatographic step after its in vitro activation. It was active on ABTS, 2,6-dimethoxyphenol (DMP), and anthraquinoid and azo dyes as reported for other fungal DyPs, but it was also able to oxidize Mn<sup>2+</sup> (as manganese peroxidases and versatile peroxidases) and veratryl alcohol (VA) (as lignin peroxidases and versatile peroxidases). This corroborated that <i>I. lacteus</i> DyPs are the only enzymes able to oxidize high redox potential dyes, VA and Mn<sup>+2</sup>. Phylogenetic analysis grouped this enzyme with other type D-DyPs from basidiomycetes. In addition to its interest for dye decolorization, the results of the transformation of softwood and hardwood lignosulfonates suggest a putative biological role of this enzyme in the degradation of phenolic lignin.https://www.mdpi.com/2309-608X/7/5/325fungioxidoreductasesDyPlignocellulosic biomasslignin |
spellingShingle | Laura Isabel de Eugenio Rosa Peces-Pérez Dolores Linde Alicia Prieto Jorge Barriuso Francisco Javier Ruiz-Dueñas María Jesús Martínez Characterization of a Dye-Decolorizing Peroxidase from <i>Irpex lacteus</i> Expressed in <i>Escherichia coli</i>: An Enzyme with Wide Substrate Specificity Able to Transform Lignosulfonates Journal of Fungi fungi oxidoreductases DyP lignocellulosic biomass lignin |
title | Characterization of a Dye-Decolorizing Peroxidase from <i>Irpex lacteus</i> Expressed in <i>Escherichia coli</i>: An Enzyme with Wide Substrate Specificity Able to Transform Lignosulfonates |
title_full | Characterization of a Dye-Decolorizing Peroxidase from <i>Irpex lacteus</i> Expressed in <i>Escherichia coli</i>: An Enzyme with Wide Substrate Specificity Able to Transform Lignosulfonates |
title_fullStr | Characterization of a Dye-Decolorizing Peroxidase from <i>Irpex lacteus</i> Expressed in <i>Escherichia coli</i>: An Enzyme with Wide Substrate Specificity Able to Transform Lignosulfonates |
title_full_unstemmed | Characterization of a Dye-Decolorizing Peroxidase from <i>Irpex lacteus</i> Expressed in <i>Escherichia coli</i>: An Enzyme with Wide Substrate Specificity Able to Transform Lignosulfonates |
title_short | Characterization of a Dye-Decolorizing Peroxidase from <i>Irpex lacteus</i> Expressed in <i>Escherichia coli</i>: An Enzyme with Wide Substrate Specificity Able to Transform Lignosulfonates |
title_sort | characterization of a dye decolorizing peroxidase from i irpex lacteus i expressed in i escherichia coli i an enzyme with wide substrate specificity able to transform lignosulfonates |
topic | fungi oxidoreductases DyP lignocellulosic biomass lignin |
url | https://www.mdpi.com/2309-608X/7/5/325 |
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